GenScript

MBP-tag Monoclonal Antibody (5B10B11)

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MBP-tag Antibody (A00190-40) in WB

Western blot analysis of MBP-tagged fusion protein using MBP-tag Antibody, mAb, Mouse (GenScript, A00190, 1 µg/mL). The signal was developed with IRDye™ 800 Conjugated Goat Anti-Mouse IgG. Predicted Size: 58 kD. Observed Size: 58 kD.

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Product Details

A00190-40

Applications

Tested Dilution

Publications

Western Blot (WB)

0.5-1 µg/mL

ELISA (ELISA)

0.1-1.0 µg/mL

Miscellaneous PubMed (MISC)

View 4 publications 4 publications

Product Specifications

Species Reactivity

Tag

Host/Isotype

Mouse / IgG1

Class

Monoclonal

Type

Antibody

Clone

5B10B11

Immunogen

Purified recombinant MBP fusion protein

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Lyophilized

Purification

Protein A

Storage buffer

PBS

Contains

0.02% sodium azide

Storage conditions

-20°C or -80°C if preferred

Shipping conditions

Ambient (domestic); Wet ice (international)

Product Specific Information

Reconstitute the lyophilized powder with deionized water (or equivalent) to an antibody concentration of 0.5 mg/ml.

Maltose binding protein (MBP) is a useful affinity tag that can increase the expression level and solubility of the MBP tagged protein. It promotes proper folding of the fusion protein, and it can be also used to prevent an insoluble form (inclusion bodies). MBP tagged protein is purified with an amylose column. The MBP tagged protein can be eluted from the column with maltose and cleaved with a specific protease to yield the purified target protein. MBP-tag Antibody, mAb, Mouse is suitable for detecting fusion proteins that contain a MBP-tag.GenScript MBP-tag Antibody, mAb, Mouse is produced from the hybridoma resulting from fusion of Sp2/0 myeloma and lymphocytes obtained from mouse immunized with purified recombinant MBP fusion protein.

Target Information

The approach of epitope tagging offers an easy and universal strategy for the identification and purification of proteins derived by recombinant DNA technology. The insertion of a Maltose Binding Protein (MBP) tag creates a stable fusion product that does not interfere with the bioactivity of the protein or with the biodistribution of the MBP-tagged product. Cleavage by factor Xa separates MBP from its partner protein.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.

Product References

Two Chloroplast Proteins Negatively Regulate Plant Drought Resistance Through Separate Pathways.

Plant physiology

Hong Y,Wang Z,Liu X,Yao J,Kong X,Shi H,Zhu JK

Sat Feb 01 00:00:00 UTC 2020

The Edwardsiella piscicida thioredoxin-like protein inhibits ASK1-MAPKs signaling cascades to promote pathogenesis during infection.

PLoS pathogens

Yang D,Liu X,Xu W,Gu Z,Yang C,Zhang L,Tan J,Zheng X,Wang Z,Quan S,Zhang Y,Liu Q

It is important that bacterium can coordinately deliver several effectors into host cells to disturb the cellular progress during infection however the precise role of effectors in host cell cytosol remains to be resolved. In this study we identified a new bacterial virulence effector from pathogenic Edwardsiella piscicida which presents conserved crystal structure to thioredoxin family members and is defined as a thioredoxin-like protein (Trxlp). Unlike the classical bacterial thioredoxins Trxl

Mon Jul 01 00:00:00 UTC 2019

A novel LRR and Ig domain-containing protein could function as an immune effector in Crassostrea gigas.

Fish & shellfish immunology

Wang X,Zhao X,Yan C,Jia Z,Lv Z,Ma C,Wang M

A variety of combinations of leucine-rich repeat (LRR) and immunoglobulin-like (Ig) domains have been found and discovered in invertebrates and vertebrates but the functions remain largely unexplored. In the present study a novel LRR and Ig domain-containing protein (LRRIG) CgLRRIG-3 was identified and characterized from oyster Crassostrea gigas. It contained two typical LRR motifs a LRRNT motif and an Ig domain and PSI-BALST and phylogeny analysis revealed that the sequence of CgLRRIG-3 was mos

Wed May 01 00:00:00 UTC 2019

Two novel LRR and Ig domain-containing proteins from oyster Crassostrea gigas function as pattern recognition receptors and induce expression of cytokines.

Fish & shellfish immunology

Wang X,Wang M,Xu Q,Xu J,Lv Z,Wang L,Song L

Leucine-rich repeat (LRR) domain and immunoglobulin (Ig) domain are both competent immune recognition modules, and the immunological roles of LRR and Ig domain containing- proteins (LRRIGs) are speculated to be multifunctional and worth investigating. In the present study, two novel LRRIGs, CgLRRIG-1 and CgLRRIG-2, were identified and characterized from oyster Crassostrea gigas. Both of them contained an N-terminal LRR region, an Ig domain, a transmembrane region, and a C-terminal cytoplasmic ta

Wed Nov 01 00:00:00 UTC 2017

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MBP-tag Monoclonal Antibody (5B10B11)

MBP-tag Antibody (A00190-40) in WB

Product Details

A00190-40

Western Blot (WB)

ELISA (ELISA)

Miscellaneous PubMed (MISC)

Species Reactivity

Host/Isotype

Class

Type

Clone

Immunogen

Conjugate

Form

Purification

Storage buffer

Contains

Storage conditions

Shipping conditions

Product Specific Information

Target Information

Performance Guarantee

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